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  2. Ligand binding assay - Wikipedia

    en.wikipedia.org/wiki/Ligand_binding_assay

    A ligand binding assay (LBA) is an assay, or an analytic procedure, which relies on the binding of ligand molecules to receptors, antibodies or other macromolecules. [1] A detection method is used to determine the presence and amount of the ligand-receptor complexes formed, and this is usually determined electrochemically or through a fluorescence detection method. [2]

  3. Methods to investigate protein–protein interactions - Wikipedia

    en.wikipedia.org/wiki/Methods_to_investigate...

    Rotating cell‑based ligand binding assay using radioactivity or fluorescence, is a recent method that measures molecular interactions in living cells in real-time. This method allows the characterization of the binding mechanism, as well as K d, k on and k off. This principle is being applied in several studies, mainly with protein ligands ...

  4. ELISA - Wikipedia

    en.wikipedia.org/wiki/ELISA

    The assay is a solid-phase type of enzyme immunoassay (EIA) to detect the presence of a ligand (commonly a protein) in a liquid sample using antibodies directed against the ligand to be measured. ELISA has been used as a diagnostic tool in medicine, plant pathology , and biotechnology , as well as a quality control check in various industries.

  5. TGF beta signaling pathway - Wikipedia

    en.wikipedia.org/wiki/TGF_beta_signaling_pathway

    The GS domain of the type I receptor consists of a series of about thirty serine-glycine repeats. [7] The binding of a TGFβ family ligand causes the rotation of the receptors so that their cytoplasmic kinase domains are arranged in a catalytically favorable orientation. The Type II receptor phosphorylates serine residues of the Type I receptor ...

  6. Ligand (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Ligand_(biochemistry)

    In DNA-ligand binding studies, the ligand can be a small molecule, ion, [1] or protein [2] which binds to the DNA double helix. The relationship between ligand and binding partner is a function of charge, hydrophobicity, and molecular structure. Binding occurs by intermolecular forces, such as ionic bonds, hydrogen bonds and Van der Waals forces.

  7. Scatchard equation - Wikipedia

    en.wikipedia.org/wiki/Scatchard_equation

    Let n be the number of binding sites for ligand on each receptor molecule, and let n represent the average number of ligands bound to a receptor. Let K d denote the dissociation constant between the ligand and receptor. The Scatchard equation is given by

  8. Hill equation (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Hill_equation_(biochemistry)

    Positively cooperative binding: Once one ligand molecule is bound to the enzyme, its affinity for other ligand molecules increases. For example, the Hill coefficient of oxygen binding to haemoglobin (an example of positive cooperativity) falls within the range of 1.7–3.2. [5] <. Negatively cooperative binding: Once one ligand molecule is ...

  9. Receptor–ligand kinetics - Wikipedia

    en.wikipedia.org/wiki/Receptorligand_kinetics

    Receptorligand binding kinetics also involves the on- and off-rates of binding. A main goal of receptorligand kinetics is to determine the concentrations of the various kinetic species (i.e., the states of the receptor and ligand) at all times, from a given set of initial concentrations and a given set of rate constants.